Intracellular reactions in single human granulocytes upon phorbol a myristate acetate activation using confocal raman microspectroscopy

Biophysical Journal

Volumn 78, Issue 5, 2000, Pages 2606-2613

  Sijtsema, Nanna M ^a,d   Tibbe, Arjan G J ^a   Segers Nolten, Ine G M J ^a   Verhoeven, Arthur J ^b   Weening, Ron S ^c   Greve, Jan ^a   Otto, Cees ^a  

^a UNIVERSITY OF TWENTE   (Netherlands)

^b CENTRAL LABORATORY   (Netherlands)

^c EMMA CHILDREN S HOSPITAL   (Netherlands)

^d RADBOUD UNIVERSITY NIJMEGEN   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME B558; MYELOPEROXIDASE; PHORBOL 13 ACETATE 12 MYRISTATE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE;

ARTICLE; CONFOCAL MICROSCOPY; GRANULOCYTE; HUMAN; HUMAN CELL; PROTEIN TRANSPORT; RAMAN SPECTROMETRY; REDUCTION;

LETHRINIDAE;

EID: 0034026758     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(00)76805-6     Document Type: Article

References (50)

1. - oxidoreductase in human neutrophils after stimulation with phorbolmyristate acetate. J. Biol. Chem. 265:924-930.
2. Babcock, G. T., R. T. Ingle, W. A. Oertling, J. C. Davis, B. A. Averill, C. L. Hulse, D. J. Stufkens, B. G. J. M. Boscher, and R. Wever. 1985. Raman characterization of human leukocyte myeloperoxidase and bovine spleen green haemoprotein. Insight into chromophore structure and evidence that the chromophores of myeloperoxidase are equivalent. Biochim. Biophys. Acta. 828:58-66.
3. Babior, B. M. 1984. Oxidants from phagocytes: agents of defence and destruction. Blood. 64:959-966.
4. Baehner, R. L., and D. G. Nathan. 1967. Leukocyte oxidase: defective activity in chronic granulomatous disease. Science. 155:835.
5. Bellavite, P. 1988. The superoxide-forming enzymatic system of the phagocytes. Free Radic. Biol. Med. 4:225-261.
6. Borregaard, N. 1988. The human neutrophil. Function and dysfunction. Eur. J. Haematol. 41:401-413.
7. Clark, R. A., B. D. Volpp, K. G. Leidal, and W. M. Nauseef. 1990. Two cytosolic components of the human neutrophil respiratory burst oxidase translocate to the plasma membrane during cell activation. J. Clin. Invest. 85:714-721.
8. phox have distinct roles in the regulation of electron flow in NADPH oxidase. J. Biol. Chem. 270:6543-6548.
9. -245 of neutrophils. Biochem. J. 204:479-485.
10. Curnutte, J. T., D. M. Whitten, and B. M. Babior. 1974. Defective superoxide production by granulocytes from patients with chronic granulomatous disease. N. Engl. J. Med. 290:593-597.
11. Dusi, S., and F. Rossi. 1993. Activation of NADPH-oxidase of human neutrophils involves the phosphorylation and the translocation of cytosolic p67phox. Biochem. J. 296:367-371.
12. Floris, R., N. Moguilevsky, G. Puppels, V. Deleersnyder, A. Jacquet, L. Garcia-Quintana, R. Renirie, A. Bollen, and R. Wever. 1995. Hemeprotein interaction in myeloperoxidase: modification of spectroscopic properties and catalytic activity by single residue mutation. J. Am. Chem. Soc. 117:3907-3912.
13. Henderson. W. R. 1991. Eosinophil peroxidase: occurrence and biological function. In Peroxidases in Chemistry and Biology. J. Everse, K. E. Everse, and M. B. Grisham, editors. CRC Press, Boca Raton, FL. 105-122.
14. 558. J. Biol. Chem 266:1627-1634.
15. Iizuka, T., S. Kanegasaki, R. Makino, T. Tanaka, and Y. Ishimura. 1985. Studies on neutrophil b-type cytochrome in situ by low temperature absorption spectroscopy. J. Biol. Chem. 260:12049-12053.
16. Jankowski, A., and S. Grinstein. 1999. A noninvasive fluorimetric procedure for measurement of membrane potential. Quantification of the NADPH oxidase-induced depolarization in activated neutrophils. J. Biol. Chem. 274:26098-26104.
17. Klebanoff, S. J. 1991. Myeloperoxidase: occurrence and biological function. In Peroxidases in Chemistry and Biology. J. Everse, K. E. Everse, and M. B. Grisham, editors. CRC Press, Boca Raton, FL. 1-36.
18. 2-halide system and granule basic proteins. J. Immunol. 143:239-244.
19. Knaus, U. G., P. G. Heyworth, T. Evans, J. T. Curnutte, and G. M. Bokoch. 1991. Regulation of phagocyte oxygen radical production by the GTP-binding protein Rac-2. Science. 254:1512-1515.
20. Kobayashi, T., J. M. Robinson, and H. Seguchi. 1998. Identification of intracellular sites of superoxide production in stimulated neutrophils. J. Cell Sci. 111:81-91.
21. Kooter, I. M., N. Moguilevsky, A. Bollen, N. M. Sijtsema, C. Otto, and R. Wever 1997. Site-directed mutagenesis of Met243, a residue of myeloperoxidase involved in the binding of the prosthetic group. J. Biol. Inorg. Chem. 2:191-197.
22. Lehrer, R. I., and M. J. Cline. 1969. Leukocyte myeloperoxidase deficiency and disseminated candidiasis - role of myeloperoxidase in resistance to Candida infection. J. Clin. Invest. 48:1478-1488.
23. Lundqvist, H., P. Follin, L. Khalfan, and C. Dahlgren. 1996. Phorbol myristate acetate-induced NADPH-oxidase activity in human neutrophils: only half the story has been told. J. Leukoc. Biol. 59: 270-279.
24. Majumdar, S., M. W. Rossi, T. Fujiki, W. A. Philips, S. Disa, C. F. Queen, R. B. Johnston Jr, O. M. Rosen, B. E. Corkey, and H. M. Korchak. 1991. Protein kinase C isotypes and signaling in neutrophils. Differential substrate specificities of a translocatable, calcium- and phospholipid-dependent β-protein kinase C and a novel calcium-independent, phospholipid-dependent protein kinase which is inhibited by long chain fatty acyl coenzyme A. J. Biol. Chem. 266:9285-9295.
25. Manoharan, R., Y. Wang, and M. S. Feld. 1996. Histochemical analysis of biological tissues using Raman spectroscopy. Spectrochim. Acta Part A. 52:215-249.
26. Nauseef, W. M. 1990. Myeloperoxidase deficiency. Hematol. Pathol. 4:165-178.
27. Oertling, W. A., H. Hoogland, G. T. Babcock, and R. Wever. 1988. Identification and properties of an oxoferryl structure in myeloperoxidase compound II. Biochemistry. 27:5395-5400.
28. Puppels, G. J., T. C. Bakker Schut, N. M. Sijtsema, M. Grond, F. Maraboeuf, C. G. de Grauw, C. G. Figdor, and J. Greve. 1995. Development and application of Raman microspectroscopic and Raman imaging techniques for cell biological studies. J. Mol. Struct. 347:477-484.
29. Puppels, G. J., W. Colier, J. H. F. Olminkhof, C. Otto, F. F. M. de Mul, and J. Greve. 1991a. Description of a highly sensitive confocal Raman microspectrometer. J. Raman Spectrosc. 22:217-225.
30. Puppels, G. J., F. F. M. de Mul, C. Otto, J. Greve, M. Robert-Nicoud, D. J. Arndt-Jovin, and T. M. Jovin. 1990. Studying single living cells and chromosomes by confocal Raman microspectroscopy. Nature. 347: 301-303.
31. Puppels, G. J., H. S. P. Garritsen, J. A. Kummer, and J. Greve. 1993. Carotenoids located in human lymphocyte subpopulations and natural killer cells by Raman microspectroscopy. Cytometry. 14:251-256.
32. Puppels, G. J., H. S. P. Garritsen, G. M. J. Segers-Nolten, F. F. M. de Mul, and J. Greve. 1991b. Raman microspectroscopic approach to the study of human granulocytes. Biophys. J. 60:1046-1056.
33. Puppels, G. J., C. A. J. Putman, B. G. de Grooth, and J. Greve. 1992. Raman microspectroscopy of chromosomal banding patterns. SPIE. 1922:145-155.
34. - -forming NADPH-oxidase of human neutrophils involves the phosphorylation and the translocation of cytosolic p67phox. Biochim. Biophys. Acta. 853:65-98.
35. 558-the flavin binding component of the phagocyte NADPH-oxidase. Science. 256:1459-1462.
36. Salmaso, B. L. N., G. J. Puppels, P. J. Caspars, R. Floris, R. Wever, and J. Greve. 1994. Resonance Raman microspectroscopic characterization of eosinophil peroxidase in human eosinophilic granulocytes. Biophys. J. 67:436-446.
37. -245 is a flavocytochrome containing Fad and the NADPH-binding site of the microbicidal oxidase of phagocytes. Biochem. J. 284:781-788.
38. Sibbett, S. S., and J. K. Hurst. 1984. Structural analysis of myeloperoxidase by resonance Raman spectroscopy. Biochemistry. 23:3007-3013.
39. Sibbett, S. S., S. J. Klebanoff, and J. K. Hurst. 1985. Characterization of the heme prosthetic group in eosinophil peroxidase. FEBS Lett. 189: 271-275.
40. 558 in human neutrophilic granulocytes. Biophys. J. 74:3250-3255.
41. Sijtsema, N. M., S. D. Wouters, C. J. de Grauw, C. Otto, and J. Greve. 1998a. A confocal direct imaging Raman microscope: design and applications in biology. Appl. Spectrosc. 52:348-355.
42. Smith, R. M., and J. T. Curnutte. 1991. Molecular basis of chronic granulomatous disease. Blood. 77:673-686.
43. Stump, R. F., G. G. Deanin, J. M. Oliver, and J. A. Shelnutt. 1987. Heme-linked ionizations of myeloperoxidase detected by Raman difference spectroscopy. A comparison with plant and yeast peroxidases. Biophys. J. 51:605-610.
44. 558, a component of the phagocyte NADPH-oxidase, is a flavoprotein. Biochem. Biophys. Res. Commun. 186:1368-1375.
45. 2 pool generated by human neutrophils. J. Biol. Chem. 259:399-405.
46. - in activated neutrophils: assembly of the NADPH-oxidase in the membrane of specific granules. Eur. J. Clin. Invest. 25:A21.
47. Vaissiere, C., V. Le Cabec, and I. Maridonneau-Parini. 1999. NADPH oxidase is functionally assembled in specific granules during activation of human neutrophils. J. Leukoc. biol. 65:629-634.
48. Wever, R., and H. Plat. 1981. Spectral properties of myeloperoxidase and its ligand complexes. Biochim. Biophys. Acta. 661:235-239.
49. Winterbourn, C. C., R. C. Garcia, and A. W. Segal. 1985. Production of the superoxide adduct of myeloperoxidase (compound III) by stimulated human neutrophils and its reactivity with hydrogen peroxide and chloride. Biochem. J. 228:583-592.
50. Yazdanbakhsh, M., C. M. Eckmann, L. Koenderman, A. J. Verhoeven, and D. Roos. 1987. Eosinophils do respond to fMLP. Blood. 70:379-383.